Immobilization of an Industrial β-Glucosidase from Aspergillus fumigatus and Its Use for Cellobiose Hydrolysis

Yepes, Clara M.; Estévez, Juliana; Arroyo, Miguel; Ladero, Miguel

doi:10.3390/pr10061225

Cited by 9 publications

(6 citation statements)

References 37 publications

(52 reference statements)

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“…Several protocols for immobilization via CLEAs [24][25][26][27] and on solid supports via multiple binding [28][29][30][31][32][33] have been reported. Covalent immobilization by a multi-point attachment was realized, for example, by using supports that expose epoxy groups [28,34,35] or functionalized amine groups with glutaraldehyde [36][37][38][39], bisepoxides [28,35], or other difunctional reagents [40]. Site-specific immobilization enables targeted immobilization and can avoid detrimental binding (e.g., if the catalytic site is facing the surface), excessive enzyme rigidification, and unspecific interactions (e.g., with active site amino acids).…”

Section: Introductionmentioning

confidence: 99%

Comparison of Four Immobilization Methods for Different Transaminases

et al. 2023

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Biocatalytic syntheses often require unfavorable conditions, which can adversely affect enzyme stability. Consequently, improving the stability of biocatalysts is needed, and this is often achieved by immobilization. In this study, we aimed to compare the stability of soluble and immobilized transaminases from different species. A cysteine in a consensus sequence was converted to a single aldehyde by the formylglycine-generating enzyme for directed single-point attachment to amine beads. This immobilization was compared to cross-linked enzyme aggregates (CLEAs) and multipoint attachments to glutaraldehyde-functionalized amine- and epoxy-beads. Subsequently, the reactivity and stability (i.e., thermal, storage, and solvent stability) of all soluble and immobilized transaminases were analyzed and compared under different conditions. The effect of immobilization was highly dependent on the type of enzyme, the immobilization strategy, and the application itself, with no superior immobilization technique identified. Immobilization of HAGA-beads often resulted in the highest activities of up to 62 U/g beads, and amine beads were best for the hexameric transaminase from Luminiphilus syltensis. Furthermore, the immobilization of transaminases enabled its reusability for at least 10 cycles, while maintaining full or high activity. Upscaled kinetic resolutions (partially performed in a SpinChemTM reactor) resulted in a high conversion, maintained enantioselectivity, and high product yields, demonstrating their applicability.

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Section: Introductionmentioning

confidence: 99%

Comparison of Four Immobilization Methods for Different Transaminases

et al. 2023

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“…To test the goodness of the proposed kinetic model, some statistical parameters were provided by the software: root main squared error (RMSE) (Equation ( 1)) measures the cumulative error between the experimental data and the fitted model, so it should tend to zero. This parameter is based on the sum of squared residuals (SSR), represented in Equation (2), that indicates the overall error present in the model, in respect of experimental data [19,36].…”

Section: Mathematical Methodsmentioning

confidence: 99%

Fumaric Acid Production by R. arrhizus NRRL 1526 Using Apple Pomace Enzymatic Hydrolysates: Kinetic Modelling

et al. 2022

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Fumaric acid is one of the most promising biorefinery platform chemicals, fruit residues being a very suitable raw material for its production in second generation biorefineries. In particular, apple pomace is a plentiful residue from the apple juice industry, with apple being the second largest fruit crop in the world, with a production that increased from 46 to 86 Mtons in the 1994–2021 period. With a global apple juice production of more than 4.5 Mtons, a similar amount of apple pomace is produced yearly. In this work, apple pomace hydrolysate has been obtained by enzymatic hydrolysis and further characterized for its content in sugars, phenolics and nitrogen using different analytic methods, based on HPLC and colorimetric techniques. Previous to the use of this hydrolysate (APH), we studied if the addition of fructose to the usual glucose-rich broth could lead to high fumaric acid yields, titers and productivities. Afterwards, APH fermentation was performed and improved using different nitrogen initial amounts, obtaining production yields (0.32 gFumaric acid/gconsumed sugar) similar to those obtained with synthetic media (0.38 gFumaric acid/gconsumed sugar). Kinetic modelling was employed to evaluate, explain, and understand the experimental values and trends of relevant components in the fermentation broth as functions of the bioprocess time, proposing a suitable reaction scheme and a non-structured, non-segregated kinetic model based on it.

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“…The release of glucose by β-glucosidases is vital because glucose is a treasure trove of energy and a crucial building block for the synthesis of biofuels. It has been demonstrated that immobilizing β-glucosidases on appropriate substrates enhances their catalytic activity, which may have consequences for a range of industrial uses, such as the generation of biofuel [41], [42], [43].…”

Section: Endoglucanases and Exoglucanasesmentioning

confidence: 99%

Enzymatic hydrolysis in food processing: biotechnological advancements, applications, and future perspectives

Akimova,

Kakimov,

Suychinov

et al. 2024

Potr. S. J. F. Sci.

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In food processing, enzymatic hydrolysis has become a revolutionary biotechnological instrument that provides consistency and sustainability that are unmatched by traditional techniques. This work thoroughly analyzes current developments in enzymatic hydrolysis and examines its uses in various food processing contexts. The biotechnological aspects—such as substrate specificity, enzyme engineering, and sustainable process optimization—are the main focus. The historical background and development of enzymatic hydrolysis in food processing are explored at the study's outset, highlighting the process's transformation from a specialized use to a critical component of contemporary biotechnological food production. A thorough literature review underscores the specificity of enzymes in dissolving various dietary components, offering insights into the biotechnological nuances controlling substrate-enzyme interactions. A careful examination of the many enzymes used in enzymatic hydrolysis and a full assessment of their uses and specificities are provided. Enzymatic hydrolysis selection criteria are outlined, taking regulatory compliance, thermostability, pH sensitivity, and substrate specificity into account. The integration of enzymatic hydrolysis into workflows for food processing is also covered, focusing on compatibility with current infrastructure and processing parameters. The case studies that demonstrate the effective use of enzymatic hydrolysis in various food production situations are the core of the research. These examples illustrate the adaptability and effectiveness of enzymatic processes in improving food quality, from developing gluten-free products to optimizing fermentation in baked goods. In its futuristic conclusion, the article imagines how enzymatic hydrolysis will continue to influence food processing in the years to come. The biotechnological viewpoint strongly emphasizes current research directions, such as integrating enzymatic processes into sustainable food production techniques and engineering enzymes for increased specificity. This biotechnological investigation highlights how enzymatic hydrolysis may completely change the food processing industry by providing accuracy, sustainability, and creativity in pursuing wholesome, nutrient-dense, and aesthetically pleasing food items.

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Immobilization of an Industrial β-Glucosidase from Aspergillus fumigatus and Its Use for Cellobiose Hydrolysis

Cited by 9 publications

References 37 publications

Comparison of Four Immobilization Methods for Different Transaminases

Comparison of Four Immobilization Methods for Different Transaminases

Fumaric Acid Production by R. arrhizus NRRL 1526 Using Apple Pomace Enzymatic Hydrolysates: Kinetic Modelling

Enzymatic hydrolysis in food processing: biotechnological advancements, applications, and future perspectives

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